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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 J+Virol
2006 ; 80
(3
): 1121-9
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A methionine-rich domain mediates CRM1-dependent nuclear export activity of Borna
disease virus phosphoprotein
#MMPMID16414989
Yanai H
; Kobayashi T
; Hayashi Y
; Watanabe Y
; Ohtaki N
; Zhang G
; de la Torre JC
; Ikuta K
; Tomonaga K
J Virol
2006[Feb]; 80
(3
): 1121-9
PMID16414989
show ga
Borna disease virus (BDV) is a nonsegmented, negative-strand RNA virus that
replicates and transcribes in the nucleus of infected cells. Recently, we have
demonstrated that BDV phosphoprotein (P) can modulate its subcellular
localization through binding to the protein X, which is encoded in the
overlapping open reading frame (T. Kobayashi et al., J. Virol. 77:8099-8107,
2003). This observation suggested a unique strategy of intracellular trafficking
of a viral protein that is essential for the formation of a functional BDV
ribonucleoprotein (RNP). However, neither the mechanism nor the consequences of
the cytoplasmic retention or nuclear export of BDV X-P complex have been
elucidated. In this study, we show that BDV P contains a bona fide nuclear export
signal (NES) and can actively shuttle between the nucleus and cytoplasm. A
transient transfection analysis of cDNA clones that mimic the BDV bicistronic X/P
mRNA revealed that the methionine-rich (MetR) domain of P is responsible for the
X-dependent cytoplasmic localization of the protein complex. Mutational and
functional analysis revealed that the methionine residues within the MetR domain
are critical for the activity of the NES of P. Furthermore, leptomycin B or small
interfering RNA for inhibition of CRM1 strongly suggested that a CRM1-dependent
pathway mediates nuclear export of P. Fluorescence loss in photobleaching
analysis confirmed the nucleocytoplasmic shuttling of P. Moreover, we revealed
that the nuclear export of P is not involved in the inhibition of the polymerase
activity by X in the BDV minireplicon system. Our results may provide a unique
strategy for the nucleocytoplasmic transport of viral RNP, which could be
critical for the formation of not only infectious virions in the cytoplasm but
also a persistent viral state in the nucleus.